Protein Structure Determination via NMR Spectral Data
Srinivas Aluru · 2005
Protein functions are determined mostly by its three dimensional structure and the structure determination is one of the top challenges in both genomics and proteomics eras. Although having been employed for a long period of time, NMR spectroscopy and X-ray crystallography are still the two main experimental methods for protein structure determination at atomic resolution. It is acknowledged that NMR protein structure determination hasn’t been able to achieve the same accuracy as X-ray crystallography does and thus X-ray crystallography remains its dominant position. Nonetheless, NMR spectroscopy complements it in many ways. Typically, structure determination via NMR spectroscopy can provide the three dimensional structure of a protein in solution under nearly physiological conditions along with dynamics information associated with the protein function. Therefore, with the advent of recent innovations such as heteronuclear NMR and cryoprobes [20], NMR spectroscopy is expected to play a more significant role in structural biology, particularly in the high-throughput structure production of the Structural Genomics Initiative [40].